ArticleThe Journal of biological chemistry2015
Structural dynamics of the glycine-binding domain of the N-methyl-D-aspartate receptor.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed, 42 citations in OpenAlex.
- Partial agonism in heteromeric GLUK2/GLUK5 kainate receptor.Proteins · 2025Article
- Bi-directional allosteric pathway in NMDA receptor activation and modulation.Nature communications · 2024Article
- Modeling and Simulation of the NMDA Receptor at Coarse-Grained and Atomistic Levels.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Single-Molecule FRET Analyses of NMDA Receptors.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Structural insights into NMDA receptor pharmacology.Biochemical Society transactions · 2023Review
- Review
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Structural Arrangement Produced by Concanavalin A Binding to Homomeric GluK2 Receptors.Membranes · 2021Article
- Single molecule FRET methodology for investigating glutamate receptors.Methods in enzymology · 2021Article
- Conformational spread and dynamics in allostery of NMDA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mechanism of modulation of AMPA receptors by TARP-γ8.The Journal of general physiology · 2020Article
- The structural arrangement and dynamics of the heteromeric GluK2/GluK5 kainate receptor as determined by smFRET.Biochimica et biophysica acta. Biomembranes · 2020Article
- Glycine Signaling in the Framework of Dopamine-Glutamate Interaction and Postsynaptic Density. Implications for Treatment-Resistant Schizophrenia.Frontiers in psychiatry · 2020Review
- Mechanistic Understanding of the Phosphorylation-Induced Conformational Rigidity at the AMPA Receptor C-terminal Domain.ACS omega · 2019Article
- The structural arrangement at intersubunit interfaces in homomeric kainate receptors.Scientific reports · 2019Article
- Activation and desensitization of ionotropic glutamate receptors by selectively triggering pre-existing motions.Neuroscience letters · 2019Review
- Dissecting diverse functions of NMDA receptors by structural biology.Current opinion in structural biology · 2019Review
- Phosphorylation Induces Conformational Rigidity at the C-Terminal Domain of AMPA Receptors.The journal of physical chemistry. B · 2019Article
- Single-Molecule FRET Methods to Study Glutamate Receptors.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Structure, function, and allosteric modulation of NMDA receptors.The Journal of general physiology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
N-Methyl-D-aspartate receptors mediate the slow component of excitatory neurotransmission in the central nervous system. These receptors are obligate heteromers containing glycine- and glutamate-binding subunits. The ligands bind to a bilobed agonist-binding domain of the receptor. Previous x-ray structures of the glycine-binding domain of NMDA receptors showed no significant changes between the partial and full agonist-bound structures. Here we have used single molecule fluorescence resonance energy transfer (smFRET) to investigate the cleft closure conformational states that the glycine-binding domain of the receptor adopts in the presence of the antagonist 5,7-dichlorokynurenic acid (DCKA), the partial agonists 1-amino-1-cyclobutanecarboxylic acid (ACBC) and L-alanine, and full agonists glycine and D-serine. For these studies, we have incorporated the unnatural amino acid p-acetyl-L-phenylalanine for specific labeling of the protein with hydrazide derivatives of fluorophores. The single molecule fluorescence resonance energy transfer data show that the agonist-binding domain can adopt a wide range of cleft closure states with significant overlap in the states occupied by ligands of varying efficacy. The difference lies in the fraction of the protein in a more closed-cleft form, with full agonists having a larger fraction in the closed-cleft form, suggesting that the ability of ligands to select for these states could dictate the extent of activation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.